Enzymatic Joining of Polynucleotides

作者：Paul L. Modrich, I Lehman · 发表于：Journal of Biological Chemistry · 年份：1970 · DOI：10.1016/s0021-9258(18)62972-2 · 被引用次数：157 · 研究领域：DNA and Nucleic Acid Chemistry、RNA and protein synthesis mechanisms、Amino Acid Enzymes and Metabolism

A new method for the assay of polynucleotide joining activity is described; it measures the conversion of 3H-labeled d(A-T) copolymer with 3'-hydroxyl and 5'-phosphoryl termini to a form resistant to exonuclease III. The method is rapid and precise and is suitable for assay of crude cell extracts. The product of the action of joining enzyme on the d(A-T) copolymer has the properties of a circular molecule. The optimal chain length of the d(A-T)n substrate is approximately 1000 nucleotides.